Research workbench
Crystal structure of a GH1 beta-glucosidase from the fungus humicola insolens
Analyse Crystal structure of a GH1 beta-glucosidase from the fungus humicola insolens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MDO
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucosidase
- UniProt
- O93784
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucosidase | protein | 477 | 44% helix, 16% strand | O93784 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.75 | 0.86 | 36 | TRS, PEG |
| 2 | 50 | 0.27 | 0.75 | 16 | empty |
Compared structures
- 4MDO · Crystal structure of a GH1 beta-glucosidase from the fungus Humicola insolens · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O93784
- Elsewhere: RCSB PDB 4MDO · PDBe 4MDO · UniProt O93784
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